Schlattner 2019 MiP2019

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Uwe Schlattner
Development of a genetically-encoded fluorescent sensor to analyze cellular energy state.

Link: MiP2019

Schlattner U, Pelosse M, Berger I (2019)

Event: MiP2019


For sensing and regulating cellular energy state, eukaryotic cells have evolved a key protein kinase, the heterotrimeric AMP-activated protein kinase (AMPK). Increasing AMP and ADP concentrations as occurring under energy stress activate AMPK. As we showed earlier, activation involves a conformational switch within the heterotrimeric kinase complex. This is exploited here for the construction of a synthetic nanosensor, AMPfret, able to report cellular energy state and allosteric AMPK activation by energy stress [1]. Based on engineered AMPK fused to fluorescent proteins, the sensor gives a direct, real-time readout of the AMPK conformational state by fluorescence resonance energy transfer (FRET). AMPfret faithfully and dynamically reports the binding of AMP and ADP to the AMPK γ-CBS sites, competed by Mg2+-free ATP. The FRET signal correlates with activation of AMPK by allosteric mechanisms and protection from dephosphorylation. As demonstrated in different cell lines, AMPfret is applicable for in vivo spatiotemporal analysis of energy state and allosteric AMPK activation.

Bioblast editor: Plangger M, Tindle-Solomon L O2k-Network Lab: FR Grenoble Schlattner U

Labels: MiParea: Instruments;methods 

Regulation: ATP 


Schlattner U()1, Pelosse M(1), and Berger I(2)
  1. Univ Grenoble Alpes INSERM U1055, Lab Fundamental Applied Bioenergetics (LBFA) SFR Environmental Systems Biology (BEeSy), Grenoble, France
  2. Bristol Synthetic Biology Centre BrisSynBio, Biomedical Sciences, Univ Bristol, Clifton, United Kingdom


  1. Pelosse M, Cottet-Rousselle C, Bidan C, Dupont A, Gupta K, Berger I, Schlattner U (2019) Synthetic energy sensor AMPfret deciphers adenylate-dependent AMPK activation mechanism. Nat Commun 10:1-13.